1qw6: Difference between revisions

Revision as of 13:57, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qw6.png

Template:STRUCTURE 1qw6

Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.

Template:ABSTRACT PUBMED 12954642

About this StructureAbout this Structure

1QW6 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms., Fedorov R, Hartmann E, Ghosh DK, Schlichting I, J Biol Chem. 2003 Nov 14;278(46):45818-25. Epub 2003 Sep 3. PMID:12954642

Page seeded by OCA on Tue Jul 29 13:57:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qw6.jpg|left|200px]]
+{{Seed}}
+[[Image:1qw6.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qw6|  PDB=1qw6  |  SCENE=  }}
-'''Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.'''
+===Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.===
-==Overview==
+<!--
-The high level of amino acid conservation and structural similarity in the immediate vicinity of the substrate binding sites of the oxygenase domains of the nitric-oxide synthase (NOS) isoforms (eNOSoxy, iNOSoxy, and nNOSoxy) make the interpretation of the structural basis of inhibitor isoform specificity a challenge and provide few clues for the design of new selective compounds. Crystal structures of iNOSoxy and nNOSoxy complexed with the inhibitors W1400 and Nomega-propyl-l-arginine provide a rationale for their isoform specificity. It involves differences outside the immediate active site as well as a conformational flexibility in the active site that allows the adoption of distinct conformations in response to interactions with the inhibitors. This flexibility is determined by isoform-specific residues outside the active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_12954642}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12954642 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12954642}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Schlichting, I.]]
 [[Category: Rat nnosoxy complex with n-omega-propyl-l-arg]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:46:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:57:01 2008''